Q08832 · GBRB3_DROME
- ProteinGamma-aminobutyric acid receptor subunit beta-like
- GeneLcch3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids496 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. Combines with the ligand-gated ion channel subunit GRD to form cation-selective GABA-gated ion channels when coexpressed in Xenopus laevis oocytes.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chloride channel complex | |
Cellular Component | GABA-A receptor complex | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | synapse | |
Cellular Component | transmembrane transporter complex | |
Molecular Function | GABA-A receptor activity | |
Molecular Function | GABA-gated chloride ion channel activity | |
Molecular Function | neurotransmitter receptor activity | |
Biological Process | chloride transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGamma-aminobutyric acid receptor subunit beta-like
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ08832
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Postsynaptic cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-258 | Extracellular | ||||
Sequence: QLQLIRCIRKDVLAGRLENVTQTISNILQGYDIRLRPNFGGEPLHVGMDLTIASFDAISEVNMDYTITMYLNQYWRDERLAFNIFGQYFDDENDDGISDVLTLSGDFAEKIWVPDTFFANDKNSFLHDVTERNKLVRLGGDGAVTYGMRFTTTLACMMDLHYYPLDSQNCTVEIESYGYTVSDVVMYWKPTPVRGVEDAELPQFTIIGYETNDRKERLATGVYQRLSLSFKLQRNIGY | ||||||
Transmembrane | 259-280 | Helical | ||||
Sequence: FVFQTYLPSILIVMLSWVSFWI | ||||||
Transmembrane | 285-306 | Helical | ||||
Sequence: TSARVALGITTVLTMTTISTGV | ||||||
Transmembrane | 318-342 | Helical | ||||
Sequence: AIDIYLVMCFVFVFAALLEYAAVNY | ||||||
Topological domain | 343-472 | Cytoplasmic | ||||
Sequence: TYWGKRAKKKIKKVKECCPGKIGKSERSETCSTTEDIIELQDVRMSPIPSLRRGTYNATLDSIGTETMNLGKFPPSFRITRNYGTGHSQLRRRAQRGISTRPRMLHALKRGASAIKATIPKIKDVNIIDK | ||||||
Transmembrane | 473-494 | Helical | ||||
Sequence: YSRMIFPISFLAFNLGYWLFYI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | Or 27 | ||||
Sequence: MTCFTRVGVSCGLFFFLLGA | ||||||
Chain | PRO_0000000454 | 21-496 | Gamma-aminobutyric acid receptor subunit beta-like | |||
Sequence: QLQLIRCIRKDVLAGRLENVTQTISNILQGYDIRLRPNFGGEPLHVGMDLTIASFDAISEVNMDYTITMYLNQYWRDERLAFNIFGQYFDDENDDGISDVLTLSGDFAEKIWVPDTFFANDKNSFLHDVTERNKLVRLGGDGAVTYGMRFTTTLACMMDLHYYPLDSQNCTVEIESYGYTVSDVVMYWKPTPVRGVEDAELPQFTIIGYETNDRKERLATGVYQRLSLSFKLQRNIGYFVFQTYLPSILIVMLSWVSFWINHEATSARVALGITTVLTMTTISTGVRSSLPRISYVKAIDIYLVMCFVFVFAALLEYAAVNYTYWGKRAKKKIKKVKECCPGKIGKSERSETCSTTEDIIELQDVRMSPIPSLRRGTYNATLDSIGTETMNLGKFPPSFRITRNYGTGHSQLRRRAQRGISTRPRMLHALKRGASAIKATIPKIKDVNIIDKYSRMIFPISFLAFNLGYWLFYILE | ||||||
Glycosylation | 39 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 176↔190 | |||||
Sequence: CMMDLHYYPLDSQNC | ||||||
Glycosylation | 189 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Interacts with Grd (alpha chain).
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length496
- Mass (Da)56,597
- Last updated2001-06-01 v2
- Checksum62C9A9E97E8DF681
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; AAA28559/AAB27090 | ||||
Sequence: G → S | ||||||
Sequence conflict | 324 | in Ref. 5; no nucleotide entry | ||||
Sequence: V → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L17436 EMBL· GenBank· DDBJ | AAA28559.1 EMBL· GenBank· DDBJ | mRNA | ||
S62717 EMBL· GenBank· DDBJ | AAB27090.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | AAS65370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY060660 EMBL· GenBank· DDBJ | AAL28208.1 EMBL· GenBank· DDBJ | mRNA |